The AlphaFold protein structure database (24 (link)) was used to predict the model of the full length ZNF410. The crystal structure of the zinc fingers ZF1–ZF5 in complex with 17-bp DNA (PDB ID: 6WMI) was superposed and compared to the predicted model. The AlphaFold model was used as a template to perform rigid body modeling. Minimal molecular dynamic simulations were performed on the flexible regions within the structure so as to explore the conformational space adopted by FL and individual constructs of ZNF140 using BILBOMD (25 ). In BILBOMD every ∼100 ps one conformational state is stored for further SAXS fitting. We record 10 000 conformers in total, varying in Rg and Dmax values for consequent SAXS fitting and multistate validation (26 (link)). Because of the dynamic and flexible character of ZNF410, a minimal ensemble search method was used to identify the multi-state model (27 (link)) required to best fit the experimental data. The scattering profile from all 10 000 models was first computed and subsequent genetic algorithm-selection operators were performed to shortlist the best models. The experimental scattering profiles from each construct were then compared with the theoretical scattering profile of the shortlisted best atomistic models generated by BILBOMD, using FOXS followed by multistate model selection by MULTIFOXS (27 (link)).